P35556 (FBN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibrillin-2

Gene names

Name:

FBN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2912 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix.
Involvement in disease	Arthrogryposis, distal, 9 (DA9) [MIM:121050]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the fibrillin family. Contains 47 EGF-like domains. Contains 9 TB (TGF-beta binding) domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone trabecula formation Inferred from sequence or structural similarity. Source: BHF-UCL embryonic limb morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of bone mineralization Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: BHF-UCL sequestering of TGFbeta in extracellular matrix Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	microfibril Traceable author statement PubMed 20855508. Source: BHF-UCL
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro extracellular matrix structural constituent Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35556-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P35556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-145: Missing.
     1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
     1507-2912: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 2912	2884	Fibrillin-2		PRO_0000007584
Regions
	Domain	111 – 142	32	EGF-like 1
	Domain	145 – 176	32	EGF-like 2
	Domain	176 – 208	33	EGF-like 3
	Domain	214 – 266	53	TB 1
	Domain	276 – 317	42	EGF-like 4; calcium-binding
	Domain	318 – 359	42	EGF-like 5; calcium-binding
	Domain	364 – 417	54	TB 2
	Domain	494 – 534	41	EGF-like 6
	Domain	535 – 574	40	EGF-like 7; calcium-binding
	Domain	575 – 616	42	EGF-like 8; calcium-binding
	Domain	617 – 657	41	EGF-like 9; calcium-binding
	Domain	658 – 698	41	EGF-like 10; calcium-binding
	Domain	704 – 756	53	TB 3
	Domain	768 – 809	42	EGF-like 11; calcium-binding
	Domain	810 – 851	42	EGF-like 12; calcium-binding
	Domain	852 – 891	40	EGF-like 13; calcium-binding
	Domain	896 – 947	52	TB 4
	Domain	955 – 996	42	EGF-like 14; calcium-binding
	Domain	1001 – 1052	52	TB 5
	Domain	1073 – 1114	42	EGF-like 15; calcium-binding
	Domain	1115 – 1157	43	EGF-like 16; calcium-binding
	Domain	1158 – 1199	42	EGF-like 17; calcium-binding
	Domain	1200 – 1241	42	EGF-like 18; calcium-binding
	Domain	1242 – 1282	41	EGF-like 19; calcium-binding
	Domain	1283 – 1324	42	EGF-like 20; calcium-binding
	Domain	1325 – 1366	42	EGF-like 21; calcium-binding
	Domain	1367 – 1407	41	EGF-like 22; calcium-binding
	Domain	1408 – 1448	41	EGF-like 23; calcium-binding
	Domain	1449 – 1490	42	EGF-like 24; calcium-binding
	Domain	1491 – 1531	41	EGF-like 25; calcium-binding
	Domain	1532 – 1572	41	EGF-like 26; calcium-binding
	Domain	1577 – 1633	57	TB 6
	Domain	1650 – 1691	42	EGF-like 27; calcium-binding
	Domain	1692 – 1733	42	EGF-like 28; calcium-binding
	Domain	1738 – 1791	54	TB 7
	Domain	1808 – 1849	42	EGF-like 29; calcium-binding
	Domain	1850 – 1891	42	EGF-like 30; calcium-binding
	Domain	1892 – 1933	42	EGF-like 31; calcium-binding
	Domain	1934 – 1972	39	EGF-like 32; calcium-binding
	Domain	1973 – 2015	43	EGF-like 33; calcium-binding
	Domain	2016 – 2055	40	EGF-like 34; calcium-binding
	Domain	2056 – 2097	42	EGF-like 35; calcium-binding
	Domain	2102 – 2155	54	TB 8
	Domain	2171 – 2212	42	EGF-like 36; calcium-binding
	Domain	2213 – 2252	40	EGF-like 37; calcium-binding
	Domain	2253 – 2293	41	EGF-like 38; calcium-binding
	Domain	2294 – 2337	44	EGF-like 39; calcium-binding
	Domain	2338 – 2379	42	EGF-like 40; calcium-binding
	Domain	2384 – 2437	54	TB 9
	Domain	2449 – 2490	42	EGF-like 41; calcium-binding
	Domain	2491 – 2531	41	EGF-like 42; calcium-binding
	Domain	2532 – 2570	39	EGF-like 43; calcium-binding
	Domain	2571 – 2613	43	EGF-like 44; calcium-binding
	Domain	2614 – 2653	40	EGF-like 45; calcium-binding
	Domain	2654 – 2694	41	EGF-like 46; calcium-binding
	Domain	2695 – 2734	40	EGF-like 47; calcium-binding
Amino acid modifications
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	1112	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	1414	1	N-linked (GlcNAc...) Potential
	Glycosylation	1529	1	N-linked (GlcNAc...) Potential
	Glycosylation	1625	1	N-linked (GlcNAc...) Potential
	Glycosylation	1714	1	N-linked (GlcNAc...) Potential
	Glycosylation	1745	1	N-linked (GlcNAc...) Potential
	Glycosylation	1756	1	N-linked (GlcNAc...) Potential
	Glycosylation	1945	1	N-linked (GlcNAc...) Potential
	Glycosylation	2120	1	N-linked (GlcNAc...) Potential
	Glycosylation	2225	1	N-linked (GlcNAc...) Potential
	Glycosylation	2808	1	N-linked (GlcNAc...) Potential
	Disulfide bond	115 ↔ 124		By similarity
	Disulfide bond	119 ↔ 130		By similarity
	Disulfide bond	132 ↔ 141		By similarity
	Disulfide bond	149 ↔ 159		By similarity
	Disulfide bond	153 ↔ 164		By similarity
	Disulfide bond	166 ↔ 175		By similarity
	Disulfide bond	180 ↔ 190		By similarity
	Disulfide bond	184 ↔ 196		By similarity
	Disulfide bond	198 ↔ 207		By similarity
	Disulfide bond	280 ↔ 292		By similarity
	Disulfide bond	287 ↔ 301		By similarity
	Disulfide bond	303 ↔ 316		By similarity
	Disulfide bond	322 ↔ 334		By similarity
	Disulfide bond	329 ↔ 343		By similarity
	Disulfide bond	345 ↔ 358		By similarity
	Disulfide bond	498 ↔ 510		By similarity
	Disulfide bond	505 ↔ 519		By similarity
	Disulfide bond	521 ↔ 533		By similarity
	Disulfide bond	539 ↔ 549		By similarity
	Disulfide bond	544 ↔ 558		By similarity
	Disulfide bond	560 ↔ 573		By similarity
	Disulfide bond	579 ↔ 591		By similarity
	Disulfide bond	586 ↔ 600		By similarity
	Disulfide bond	602 ↔ 615		By similarity
	Disulfide bond	621 ↔ 632		By similarity
	Disulfide bond	627 ↔ 641		By similarity
	Disulfide bond	643 ↔ 656		By similarity
	Disulfide bond	662 ↔ 673		By similarity
	Disulfide bond	668 ↔ 682		By similarity
	Disulfide bond	684 ↔ 697		By similarity
	Disulfide bond	772 ↔ 784		By similarity
	Disulfide bond	779 ↔ 793		By similarity
	Disulfide bond	795 ↔ 808		By similarity
	Disulfide bond	814 ↔ 826		By similarity
	Disulfide bond	821 ↔ 835		By similarity
	Disulfide bond	837 ↔ 850		By similarity
	Disulfide bond	856 ↔ 866		By similarity
	Disulfide bond	861 ↔ 875		By similarity
	Disulfide bond	877 ↔ 890		By similarity
	Disulfide bond	959 ↔ 971		By similarity
	Disulfide bond	966 ↔ 980		By similarity
	Disulfide bond	982 ↔ 995		By similarity
	Disulfide bond	1077 ↔ 1089		By similarity
	Disulfide bond	1084 ↔ 1098		By similarity
	Disulfide bond	1100 ↔ 1113		By similarity
	Disulfide bond	1119 ↔ 1131		By similarity
	Disulfide bond	1126 ↔ 1140		By similarity
	Disulfide bond	1142 ↔ 1156		By similarity
	Disulfide bond	1162 ↔ 1174		By similarity
	Disulfide bond	1169 ↔ 1183		By similarity
	Disulfide bond	1185 ↔ 1198		By similarity
	Disulfide bond	1204 ↔ 1216		By similarity
	Disulfide bond	1211 ↔ 1225		By similarity
	Disulfide bond	1227 ↔ 1240		By similarity
	Disulfide bond	1246 ↔ 1257		By similarity
	Disulfide bond	1253 ↔ 1266		By similarity
	Disulfide bond	1268 ↔ 1281		By similarity
	Disulfide bond	1287 ↔ 1299		By similarity
	Disulfide bond	1294 ↔ 1308		By similarity
	Disulfide bond	1310 ↔ 1323		By similarity
	Disulfide bond	1329 ↔ 1341		By similarity
	Disulfide bond	1336 ↔ 1350		By similarity
	Disulfide bond	1352 ↔ 1365		By similarity
	Disulfide bond	1371 ↔ 1384		By similarity
	Disulfide bond	1378 ↔ 1393		By similarity
	Disulfide bond	1395 ↔ 1406		By similarity
	Disulfide bond	1412 ↔ 1425		By similarity
	Disulfide bond	1419 ↔ 1434		By similarity
	Disulfide bond	1436 ↔ 1447		By similarity
	Disulfide bond	1453 ↔ 1465		By similarity
	Disulfide bond	1460 ↔ 1474		By similarity
	Disulfide bond	1476 ↔ 1489		By similarity
	Disulfide bond	1495 ↔ 1506		By similarity
	Disulfide bond	1501 ↔ 1515		By similarity
	Disulfide bond	1517 ↔ 1530		By similarity
	Disulfide bond	1536 ↔ 1547		By similarity
	Disulfide bond	1542 ↔ 1556		By similarity
	Disulfide bond	1558 ↔ 1571		By similarity
	Disulfide bond	1654 ↔ 1666		By similarity
	Disulfide bond	1661 ↔ 1675		By similarity
	Disulfide bond	1677 ↔ 1690		By similarity
	Disulfide bond	1696 ↔ 1708		By similarity
	Disulfide bond	1703 ↔ 1717		By similarity
	Disulfide bond	1719 ↔ 1732		By similarity
	Disulfide bond	1812 ↔ 1824		By similarity
	Disulfide bond	1819 ↔ 1833		By similarity
	Disulfide bond	1835 ↔ 1848		By similarity
	Disulfide bond	1854 ↔ 1867		By similarity
	Disulfide bond	1861 ↔ 1876		By similarity
	Disulfide bond	1878 ↔ 1890		By similarity
	Disulfide bond	1896 ↔ 1908		By similarity
	Disulfide bond	1903 ↔ 1917		By similarity
	Disulfide bond	1919 ↔ 1932		By similarity
	Disulfide bond	1938 ↔ 1948		By similarity
	Disulfide bond	1943 ↔ 1957		By similarity
	Disulfide bond	1959 ↔ 1971		By similarity
	Disulfide bond	1977 ↔ 1990		By similarity
	Disulfide bond	1985 ↔ 1999		By similarity
	Disulfide bond	2001 ↔ 2014		By similarity
	Disulfide bond	2020 ↔ 2032		By similarity
	Disulfide bond	2027 ↔ 2041		By similarity
	Disulfide bond	2043 ↔ 2054		By similarity
	Disulfide bond	2060 ↔ 2072		By similarity
	Disulfide bond	2067 ↔ 2081		By similarity
	Disulfide bond	2083 ↔ 2096		By similarity
	Disulfide bond	2175 ↔ 2187		By similarity
	Disulfide bond	2182 ↔ 2196		By similarity
	Disulfide bond	2198 ↔ 2211		By similarity
	Disulfide bond	2217 ↔ 2228		By similarity
	Disulfide bond	2223 ↔ 2237		By similarity
	Disulfide bond	2239 ↔ 2251		By similarity
	Disulfide bond	2257 ↔ 2268		By similarity
	Disulfide bond	2264 ↔ 2277		By similarity
	Disulfide bond	2279 ↔ 2292		By similarity
	Disulfide bond	2298 ↔ 2312		By similarity
	Disulfide bond	2305 ↔ 2321		By similarity
	Disulfide bond	2323 ↔ 2336		By similarity
	Disulfide bond	2342 ↔ 2354		By similarity
	Disulfide bond	2349 ↔ 2363		By similarity
	Disulfide bond	2365 ↔ 2378		By similarity
	Disulfide bond	2453 ↔ 2465		By similarity
	Disulfide bond	2460 ↔ 2474		By similarity
	Disulfide bond	2476 ↔ 2489		By similarity
	Disulfide bond	2495 ↔ 2506		By similarity
	Disulfide bond	2502 ↔ 2515		By similarity
	Disulfide bond	2517 ↔ 2530		By similarity
	Disulfide bond	2536 ↔ 2547		By similarity
	Disulfide bond	2543 ↔ 2556		By similarity
	Disulfide bond	2558 ↔ 2569		By similarity
	Disulfide bond	2575 ↔ 2588		By similarity
	Disulfide bond	2582 ↔ 2597		By similarity
	Disulfide bond	2599 ↔ 2612		By similarity
	Disulfide bond	2618 ↔ 2628		By similarity
	Disulfide bond	2624 ↔ 2637		By similarity
	Disulfide bond	2639 ↔ 2652		By similarity
	Disulfide bond	2658 ↔ 2669		By similarity
	Disulfide bond	2664 ↔ 2678		By similarity
	Disulfide bond	2680 ↔ 2693		By similarity
	Disulfide bond	2699 ↔ 2710		By similarity
	Disulfide bond	2706 ↔ 2719		By similarity
	Disulfide bond	2721 ↔ 2733		By similarity
Natural variations
	Alternative sequence	113 – 145	33	Missing in isoform 2.		VSP_037369
	Alternative sequence	1491 – 1506	16	DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2.		VSP_037370
	Alternative sequence	1507 – 2912	1406	Missing in isoform 2.		VSP_037371
	Natural variant	391	1	E → K in DA9.		VAR_015851
	Natural variant	594	1	T → S. Ref.1 Ref.8		VAR_054979
	Natural variant	681	1	R → H. Ref.8		VAR_054980
	Natural variant	754	1	G → S in DA9. Ref.12		VAR_058364
	Natural variant	965	1	V → I. Ref.7 Ref.8 Ref.11 Corresponds to variant rs154001 [ dbSNP | Ensembl ].		VAR_002349
	Natural variant	1057	1	G → D in DA9. Ref.8 Ref.11		VAR_054981
	Natural variant	1091	1	N → S in DA9. Ref.12		VAR_058365
	Natural variant	1093	1	I → T in DA9. Ref.8 Ref.11		VAR_054982
	Natural variant	1115	1	D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. Ref.9 Ref.12		VAR_010739
	Natural variant	1122	1	S → P in DA9. Ref.12		VAR_058366
	Natural variant	1142	1	C → F in DA9. Ref.10 Ref.11		VAR_010740
	Natural variant	1142	1	C → R in DA9. Ref.12		VAR_058367
	Natural variant	1146	1	Y → C in DA9. Ref.12		VAR_058368
	Natural variant	1156	1	C → F in DA9. Ref.12		VAR_058369
	Natural variant	1161	1	E → K in DA9. Ref.12		VAR_058370
	Natural variant	1179	1	G → C in DA9. Ref.11		VAR_054983
	Natural variant	1198	1	C → Y in DA9. Ref.11		VAR_054984
	Natural variant	1240	1	C → R in DA9. Ref.11		VAR_054985
	Natural variant	1246	1	C → F in DA9. Ref.12		VAR_058371
	Natural variant	1253	1	C → W in DA9. Ref.10 Ref.11 Corresponds to variant rs28931602 [ dbSNP | Ensembl ].		VAR_010741
	Natural variant	1253	1	C → Y in DA9. Ref.7 Ref.11		VAR_002350
	Natural variant	1257	1	C → W in DA9. Ref.11		VAR_054986
	Natural variant	1268	1	C → R in DA9. Ref.11		VAR_054987
	Natural variant	1384	1	C → F in DA9. Ref.12		VAR_058372
	Natural variant	1384	1	C → Y in DA9. Ref.12		VAR_058373
	Natural variant	1408	1	D → N in DA9. Ref.12		VAR_058374
	Natural variant	1425	1	C → R in DA9. Ref.12		VAR_058375
	Natural variant	1434	1	C → S in DA9. Ref.7 Ref.11		VAR_002351
	Natural variant	1772	1	W → G. Ref.1 Ref.8		VAR_054988
	Natural variant	2062	1	E → V Found in a renal cell carcinoma case; somatic mutation. Ref.13		VAR_064705
	Natural variant	2266	1	F → L. Ref.1 Ref.8		VAR_054989
	Natural variant	2278	1	T → M. Corresponds to variant rs2307109 [ dbSNP | Ensembl ].		VAR_055415
	Natural variant	2311	1	M → V. Corresponds to variant rs32209 [ dbSNP | Ensembl ].		VAR_055416
	Natural variant	2428	1	P → T. Ref.8 Corresponds to variant rs1801169 [ dbSNP | Ensembl ].		VAR_016143
	Natural variant	2580	1	S → L. Ref.1 Corresponds to variant rs2291628 [ dbSNP | Ensembl ].		VAR_055417
	Natural variant	2581	1	L → S. Corresponds to variant rs2291628 [ dbSNP | Ensembl ].		VAR_054990
	Natural variant	2771	1	S → P. Ref.1 Ref.8 Corresponds to variant rs1801170 [ dbSNP | Ensembl ].		VAR_014664
Experimental info
	Sequence conflict	146	1	I → L in BAG62163. Ref.2
	Sequence conflict	192 – 195	4	GPNR → AQP in AAA18950. Ref.1
	Sequence conflict	243	1	I → T in AAA18950. Ref.1
	Sequence conflict	243	1	I → T in BAG62163. Ref.2
	Sequence conflict	1161	1	E → G in AAA18950. Ref.1
	Sequence conflict	1161	1	E → G in CAB56757. Ref.4
	Sequence conflict	1244	1	D → G in BAG62163. Ref.2
	Sequence conflict	1409	1	L → R in CAB56757. Ref.4
	Sequence conflict	1503	1	F → S in AAA18950. Ref.1
	Sequence conflict	2584	1	A → G in AAA18950. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 26, 2009. Version 3. Checksum: 0F0D78319E9911E6	FASTA	2,912	314,775
	10 20 30 40 50 60 MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA TAGSEGGFLA 70 80 90 100 110 120 PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG 130 140 150 160 170 180 DGFCSRPNMC TCSSGQISST CGSKSIQQCS VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC 190 200 210 220 230 240 ENGCQNGGRC IGPNRCACVY GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC 250 260 270 280 290 300 ATIGRAWGHP CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE 310 320 330 340 350 360 CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV TSTDGSRCID 370 380 390 400 410 420 QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT IPEACPVRGS EEYRRLCMDG 430 440 450 460 470 480 LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG 490 500 510 520 530 540 QGPIITGLTI LNQTIDICKH HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT 550 560 570 580 590 600 SNPCTNGDCV NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC 610 620 630 640 650 660 ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA PNGRYCTDVD 670 680 690 700 710 720 ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT HMRSTCYGGI KKGVCVRPFP 730 740 750 760 770 780 GAVTKSECCC ANPDYGFGEP CQPCPAKNSA EFHGLCSSGV GITVDGRDIN ECALDPDICA 790 800 810 820 830 840 NGICENLRGS YRCNCNSGYE PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG 850 860 870 880 890 900 YVFRTETETC EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL 910 920 930 940 950 960 NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG VTCEDVNECE 970 980 990 1000 1010 1020 VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM EQCYLKWDED ECIHPVPGKF 1030 1040 1050 1060 1070 1080 RMDACCCAVG AAWGTECEEC PKPGTKEYET LCPRGAGFAN RGDVLTGRPF YKDINECKAF 1090 1100 1110 1120 1130 1140 PGMCTYGKCR NTIGSFKCRC NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC 1150 1160 1170 1180 1190 1200 ECFEGYESGF MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD 1210 1220 1230 1240 1250 1260 INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN GGCDTQCTNS 1270 1280 1290 1300 1310 1320 EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT NIPGEYRCLC YDGFMASMDM 1330 1340 1350 1360 1370 1380 KTCIDVNECD LNSNICMFGE CENTKGSFIC HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM 1390 1400 1410 1420 1430 1440 HASCLNIPGS FKCSCREGWI GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF 1450 1460 1470 1480 1490 1500 TGDGFTCSDV DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI 1510 1520 1530 1540 1550 1560 CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT PGRYECNCPP 1570 1580 1590 1600 1610 1620 DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG VSRSSCCCSL GKAWGNPCET 1630 1640 1650 1660 1670 1680 CPPVNSTEYY TLCPGGEGFR PNPITIILED IDECQELPGL CQGGNCINTF GSFQCECPQG 1690 1700 1710 1720 1730 1740 YYLSEDTRIC EDIDECFAHP GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC 1750 1760 1770 1780 1790 1800 YRSYNGTTCE NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD 1810 1820 1830 1840 1850 1860 IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED IDECSNGDNL 1870 1880 1890 1900 1910 1920 CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP NVCSHGLCVD LQGSYQCICH 1930 1940 1950 1960 1970 1980 NGFKASQDQT MCMDVDECER HPCGNGTCKN TVGSYNCLCY PGFELTHNND CLDIDECSSF 1990 2000 2010 2020 2030 2040 FGQVCRNGRC FNEIGSFKCL CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR 2050 2060 2070 2080 2090 2100 CICPPGYEVK SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR 2110 2120 2130 2140 2150 2160 QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA FQDLCPYGHG 2170 2180 2190 2200 2210 2220 TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM GYNLDYTGVR CVDTDECSIG 2230 2240 2250 2260 2270 2280 NPCGNGTCTN VIGSFECNCN EGFEPGPMMN CEDINECAQN PLLCAFRCMN TFGSYECTCP 2290 2300 2310 2320 2330 2340 IGYALREDQK MCKDLDECAE GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN 2350 2360 2370 2380 2390 2400 ECRTKPGICE NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS 2410 2420 2430 2440 2450 2460 SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI DECKVMPNLC 2470 2480 2490 2500 2510 2520 TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK PCNYICKNTE GSYQCSCPRG 2530 2540 2550 2560 2570 2580 YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT LGGFTCKCPP GFTQHHTACI DNNECGSQPS 2590 2600 2610 2620 2630 2640 LCGAKGICQN TPGSFSCECQ RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP 2650 2660 2670 2680 2690 2700 QGYIQHYQWN QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS 2710 2720 2730 2740 2750 2760 SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE VDEENALSPE 2770 2780 2790 2800 2810 2820 ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD SPVNMKFNLS HLGSKEHILE 2830 2840 2850 2860 2870 2880 LRPAIQPLNN HIRYVISQGN DDSVFRIHQR NGLSYLHTAK KKLMPGTYTL EITSIPLYKK 2890 2900 2910 KELKKLEESN EDDYLLGELG EALRMRLQIQ LY
	Isoform 2 [UniParc]. Checksum: 2B6620CFCA6F7A72	FASTA	1,473	157,690
	10 20 30 40 50 60 MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA TAGSEGGFLA 70 80 90 100 110 120 PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG WKTLPGGNQC IVIQQCSVRC 130 140 150 160 170 180 MNGGTCADDH CQCQKGYIGT YCGQPVCENG CQNGGRCIGP NRCACVYGFT GPQCERDYRT 190 200 210 220 230 240 GPCFTQVNNQ MCQGQLTGIV CTKTLCCATI GRAWGHPCEM CPAQPQPCRR GFIPNIRTGA 250 260 270 280 290 300 CQDVDECQAI PGICQGGNCI NTVGSFECRC PAGHKQSETT QKCEDIDECS IIPGICETGE 310 320 330 340 350 360 CSNTVGSYFC VCPRGYVTST DGSRCIDQRT GMCFSGLVNG RCAQELPGRM TKMQCCCEPG 370 380 390 400 410 420 RCWGIGTIPE ACPVRGSEEY RRLCMDGLPM GGIPGSAGSR PGGTGGNGFA PSGNGNGYGP 430 440 450 460 470 480 GGTGFIPIPG GNGFSPGVGG AGVGAGGQGP IITGLTILNQ TIDICKHHAN LCLNGRCIPT 490 500 510 520 530 540 VSSYRCECNM GYKQDANGDC IDVDECTSNP CTNGDCVNTP GSYYCKCHAG FQRTPTKQAC 550 560 570 580 590 600 IDIDECIQNG VLCKNGRCVN TDGSFQCICN AGFELTTDGK NCVDHDECTT TNMCLNGMCI 610 620 630 640 650 660 NEDGSFKCIC KPGFVLAPNG RYCTDVDECQ TPGICMNGHC INSEGSFRCD CPPGLAVGMD 670 680 690 700 710 720 GRVCVDTHMR STCYGGIKKG VCVRPFPGAV TKSECCCANP DYGFGEPCQP CPAKNSAEFH 730 740 750 760 770 780 GLCSSGVGIT VDGRDINECA LDPDICANGI CENLRGSYRC NCNSGYEPDA SGRNCIDIDE 790 800 810 820 830 840 CLVNRLLCDN GLCRNTPGSY SCTCPPGYVF RTETETCEDI NECESNPCVN GACRNNLGSF 850 860 870 880 890 900 NCECSPGSKL SSTGLICIDS LKGTCWLNIQ DSRCEVNING ATLKSECCAT LGAAWGSPCE 910 920 930 940 950 960 RCELDTACPR GLARIKGVTC EDVNECEVFP GVCPNGRCVN SKGSFHCECP EGLTLDGTGR 970 980 990 1000 1010 1020 VCLDIRMEQC YLKWDEDECI HPVPGKFRMD ACCCAVGAAW GTECEECPKP GTKEYETLCP 1030 1040 1050 1060 1070 1080 RGAGFANRGD VLTGRPFYKD INECKAFPGM CTYGKCRNTI GSFKCRCNSG FALDMEERNC 1090 1100 1110 1120 1130 1140 TDIDECRISP DLCGSGICVN TPGSFECECF EGYESGFMMM KNCMDIDECE RNPLLCRGGT 1150 1160 1170 1180 1190 1200 CVNTEGSFQC DCPLGHELSP SREDCVDINE CSLSDNLCRN GKCVNMIGTY QCSCNPGYQA 1210 1220 1230 1240 1250 1260 TPDRQGCTDI DECMIMNGGC DTQCTNSEGS YECSCSEGYA LMPDGRSCAD IDECENNPDI 1270 1280 1290 1300 1310 1320 CDGGQCTNIP GEYRCLCYDG FMASMDMKTC IDVNECDLNS NICMFGECEN TKGSFICHCQ 1330 1340 1350 1360 1370 1380 LGYSVKKGTT GCTDVDECEI GAHNCDMHAS CLNIPGSFKC SCREGWIGNG IKCIDLDECS 1390 1400 1410 1420 1430 1440 NGTHQCSINA QCVNTPGSYR CACSEGFTGD GFTCSDVDEC AENINLCENG QCLNVPGAYR 1450 1460 1470 CECEMGFTPA SDSRSCQGGS PGFQLIFKLD QPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices." Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F. J. Cell Biol. 124:855-863(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes." Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W. Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1). Tissue: Aortic endothelium.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly." Putnam E.A., Zhang H., Ramirez F., Milewicz D.M. Nat. Genet. 11:456-458(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DA9 TYR-1253 AND SER-1434, VARIANT ILE-965.
[8]	"Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development." Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M. Am. J. Med. Genet. 78:350-355(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DA9 ASP-1057 AND THR-1093, VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
[9]	"A single mutation that results in an Asp-to-His substitution and partial exon skipping in a family with congenital contractural arachnodactyly." Babcock D., Gasner C., Francke U., Maslen C. Hum. Genet. 103:22-28(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DA9 HIS-1115.
[10]	"Two novel fibrillin-2 mutations in congenital contractural arachnodactyly." Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M. Am. J. Med. Genet. 92:7-12(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DA9 PHE-1142 AND TRP-1253.
[11]	"Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype." Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A., Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K., Ades L.C., Milewicz D.M. Hum. Mutat. 19:39-48(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DA9 ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, VARIANT ILE-965.
[12]	"Comprehensive clinical and molecular assessment of 32 probands with congenital contractural arachnodactyly: report of 14 novel mutations and review of the literature." Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M., Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H., Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C., Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M. Hum. Mutat. 30:334-341(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DA9 SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146; PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
[13]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-2062.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03272 mRNA. Translation: AAA18950.1. AK300440 mRNA. Translation: BAG62163.1. AC025169 Genomic DNA. No translation available. AC034235 Genomic DNA. No translation available. AC113387 Genomic DNA. No translation available. X62009 mRNA. Translation: CAB56757.1. AB209735 mRNA. Translation: BAD92972.1.
IPI	IPI00019439. IPI00930504.
PIR	A54105.
RefSeq	NP_001990.2. NM_001999.3.
UniGene	Hs.519294.
3D structure databases
ProteinModelPortal	P35556.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35556. 1 interaction.
STRING	9606.ENSP00000262464.
PTM databases
PhosphoSite	P35556.
Polymorphism databases
DMDM	238054385.
Proteomic databases
PaxDb	P35556.
PRIDE	P35556.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262464; ENSP00000262464; ENSG00000138829. ENST00000508053; ENSP00000424571; ENSG00000138829.
GeneID	2201.
KEGG	hsa:2201.
UCSC	uc003kuu.3. human.
Organism-specific databases
CTD	2201.
GeneCards	GC05M127621.
H-InvDB	HIX0005141. HIX0137461.
HGNC	HGNC:3604. FBN2.
HPA	CAB026401. HPA012853.
MIM	121050. phenotype. 612570. gene.
neXtProt	NX_P35556.
Orphanet	115. Congenital contractural arachnodactyly.
PharmGKB	PA28017.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000231768.
HOVERGEN	HBG005643.
InParanoid	P35556.
OMA	SGRNCID.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P35556.
Bgee	P35556.
CleanEx	HS_FBN2.
Genevestigator	P35556.
GermOnline	ENSG00000138829. Homo sapiens.
Family and domain databases
Gene3D	3.90.290.10. 9 hits.
InterPro	IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR011398. FBN. IPR017878. TB_dom. [Graphical view]
PANTHER	PTHR24039:SF0. PTHR24039:SF0. 1 hit.
Pfam	PF12662. cEGF. 1 hit. PF07645. EGF_CA. 41 hits. PF00683. TB. 9 hits. [Graphical view]
PIRSF	PIRSF036312. Fibrillin. 1 hit.
SMART	SM00181. EGF. 3 hits. SM00179. EGF_CA. 43 hits. [Graphical view]
SUPFAM	SSF57581. Fibril-assoc. 9 hits.
PROSITE	PS00010. ASX_HYDROXYL. 43 hits. PS00022. EGF_1. 2 hits. PS01186. EGF_2. 37 hits. PS50026. EGF_3. 45 hits. PS01187. EGF_CA. 43 hits. PS51364. TB. 9 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	2201.
NextBio	8895.
SOURCE	Search...

Entry information

Entry name

FBN2_HUMAN

Accession

Primary (citable) accession number: P35556
Secondary accession number(s): B4DU01, Q59ES6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.